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Structure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel
Zhao, Haiyan Speir, Jeffrey A. Matsui, Tsutomu Lin, Zihan Liang, Lingfei Lynn, Anna Y. Varnado, Brittany Weiss, Thomas M. Tang, Liang
Zhao, Haiyan
Speir, Jeffrey A.
Matsui, Tsutomu
Lin, Zihan
Liang, Lingfei
Lynn, Anna Y.
Varnado, Brittany
Weiss, Thomas M.
Tang, Liang
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Abstract
The multi-layered cell envelope structure of Gram-negative bacteria represents significant physical and chemical barriers for short-tailed phages to inject phage DNA into the host cytoplasm. Here we show that a DNA-injection protein of bacteriophage Sf6, gp12, forms a 465-kDa, decameric assembly in vitro. The electron microscopic structure of the gp12 assembly shows a ~150-Å, mushroom-like architecture consisting of a crown domain and a tube-like domain, which embraces a 25-Å-wide channel that could precisely accommodate dsDNA. The constricted channel suggests that gp12 mediates rapid, uni-directional injection of phage DNA into host cells by providing a molecular conduit for DNA translocation. The assembly exhibits a 10-fold symmetry, which may be a common feature among DNAinjection proteins of P22-like phages and may suggest a symmetry mismatch with respect to the 6-fold symmetric phage tail. The gp12 monomer is highly flexible in solution, supporting a mechanism for translocation of the protein through the conduit of the phage tail toward the host cell envelope, where it assembles into a DNA-injection device.
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2016-02-16
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Public Library of Science
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Structure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel
Haiyan Zhao, Jeffrey A. Speir, Tsutomu Matsui, Zihan Lin, Lingfei Liang, Anna Y. Lynn, Brittany Varnado, Thomas M. Weiss, Liang Tang
PLoS One. 2016; 11(2): e0149337. Published online 2016 February 16. doi: 10.1371/journal.pone.0149337